7T7T

Structure of TSK/BRU1 bound to histone H3.1

Summary for 7T7T

• Entry DOI: 10.2210/pdb7t7t/pdb
• Descriptor: Protein TONSOKU, Histone H3.1 (3 entities in total)
• Functional Keywords: epigenetic protein, h3.1 reader, nucleosome, nuclear protein
• Biological source: Citrus unshiu (Satsuma mandarin, Citrus nobilis var. unshiu); More
• Total number of polymer chains: 4
• Total formula weight: 134863.08

Authors

Davarinejad, H.,Couture, J.F. (deposition date: 2021-12-15, release date: 2022-03-30, Last modification date: 2024-11-06)

Primary citation

Davarinejad, H.,Huang, Y.C.,Mermaz, B.,LeBlanc, C.,Poulet, A.,Thomson, G.,Joly, V.,Munoz, M.,Arvanitis-Vigneault, A.,Valsakumar, D.,Villarino, G.,Ross, A.,Rotstein, B.H.,Alarcon, E.I.,Brunzelle, J.S.,Voigt, P.,Dong, J.,Couture, J.F.,Jacob, Y.
The histone H3.1 variant regulates TONSOKU-mediated DNA repair during replication.
Science, 375:1281-1286, 2022

PubMed Abstract: The tail of replication-dependent histone H3.1 varies from that of replication-independent H3.3 at the amino acid located at position 31 in plants and animals, but no function has been assigned to this residue to demonstrate a unique and conserved role for H3.1 during replication. We found that TONSOKU (TSK/TONSL), which rescues broken replication forks, specifically interacts with H3.1 via recognition of alanine 31 by its tetratricopeptide repeat domain. Our results indicate that genomic instability in the absence of ATXR5/ATXR6-catalyzed histone H3 lysine 27 monomethylation in plants depends on H3.1, TSK, and DNA polymerase theta (Pol θ). This work reveals an H3.1-specific function during replication and a common strategy used in multicellular eukaryotes for regulating post-replicative chromatin maturation and TSK, which relies on histone monomethyltransferases and reading of the H3.1 variant.

PubMed: 35298257
DOI: 10.1126/science.abm5320

Experimental method

X-RAY DIFFRACTION (3.17 Å)